메뉴 건너뛰기




Volumn 290, Issue 31, 2015, Pages 19044-19054

Exchange factor TBL1 and arginine methyltransferase PRMT6 cooperate in protecting g protein pathway suppressor 2 (GPS2) from proteasomal degradation

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; AMINO ACIDS; PROTEINS;

EID: 84940570848     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.637660     Document Type: Article
Times cited : (17)

References (49)
  • 1
    • 0029860455 scopus 로고    scopus 로고
    • Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein-and mitogen-activated protein kinase-mediated signal transduction in yeast and mammalian cells
    • Spain, B. H., Bowdish, K. S., Pacal, A. R., Staub, S. F., Koo, D., Chang, C. Y., Xie, W., and Colicelli, J. (1996) Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11), suppress G-protein-and mitogen-activated protein kinase-mediated signal transduction in yeast and mammalian cells. Mol. Cell. Biol. 16, 6698-6706
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6698-6706
    • Spain, B.H.1    Bowdish, K.S.2    Pacal, A.R.3    Staub, S.F.4    Koo, D.5    Chang, C.Y.6    Xie, W.7    Colicelli, J.8
  • 3
    • 0034051288 scopus 로고    scopus 로고
    • AMF-1/Gps2 binds p300 and enhances its interaction with papillomavirus E2 proteins
    • Peng, Y. C., Breiding, D. E., Sverdrup, F., Richard, J., and Androphy, E. J. (2000) AMF-1/Gps2 binds p300 and enhances its interaction with papillomavirus E2 proteins. J. Virol. 74, 5872-5879
    • (2000) J. Virol. , vol.74 , pp. 5872-5879
    • Peng, Y.C.1    Breiding, D.E.2    Sverdrup, F.3    Richard, J.4    Androphy, E.J.5
  • 5
    • 46749108756 scopus 로고    scopus 로고
    • Cytological characterization of th e tandem repetitive sequences and their methylation status in the Antirrhinum majus genome
    • Zhang, D., Yang, Q., Ding, Y., Cao, X., Xue, Y., and Cheng, Z. (2008) Cytological characterization of th e tandem repetitive sequences and their methylation status in the Antirrhinum majus genome. Genomics 92, 107-114
    • (2008) Genomics , vol.92 , pp. 107-114
    • Zhang, D.1    Yang, Q.2    Ding, Y.3    Cao, X.4    Xue, Y.5    Cheng, Z.6
  • 7
    • 29244488526 scopus 로고    scopus 로고
    • Formation of hMSH4-hMSH5 heterocomplex is a prerequisite for subsequent GPS2 recruitment
    • Lee, T. H., Yi, W., Griswold, M. D., Zhu, F., and Her, C. (2006) Formation of hMSH4-hMSH5 heterocomplex is a prerequisite for subsequent GPS2 recruitment. DNA Repair 5, 32-42
    • (2006) DNA Repair , vol.5 , pp. 32-42
    • Lee, T.H.1    Yi, W.2    Griswold, M.D.3    Zhu, F.4    Her, C.5
  • 10
    • 0036211850 scopus 로고    scopus 로고
    • The N-CoRHDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2
    • Zhang, J., Kalkum, M., Chait, B. T., and Roeder, R. G. (2002) The N-CoRHDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2. Mol. Cell 9, 611-623
    • (2002) Mol. Cell , vol.9 , pp. 611-623
    • Zhang, J.1    Kalkum, M.2    Chait, B.T.3    Roeder, R.G.4
  • 12
    • 43749095196 scopus 로고    scopus 로고
    • G-protein pathway suppressor 2 (GPS2) interacts with the regulatory factor X4 variant 3 (RFX4-v3) and functions as a transcriptional co-activator
    • Zhang, D., Harry, G. J., Blackshear, P. J., and Zeldin, D. C. (2008) G-protein pathway suppressor 2 (GPS2) interacts with the regulatory factor X4 variant 3 (RFX4-v3) and functions as a transcriptional co-activator. J. Biol. Chem. 283, 8580-859 0
    • (2008) J. Biol. Chem. , vol.283 , pp. 8580-8590
    • Zhang, D.1    Harry, G.J.2    Blackshear, P.J.3    Zeldin, D.C.4
  • 13
    • 84922353555 scopus 로고    scopus 로고
    • The optimal corepressor function of nuclear receptor corepressor (NCoR) fo r peroxisome proliferator-activated receptor- requires G-protein pathway suppressor 2
    • Guo, C., Li, Y., Gow, C. H., Wong, M., Zha, J., Yan, C., Liu, H., Wang, Y., Burris, T. P., and Zhang, J. (2015) The optimal corepressor function of nuclear receptor corepressor (NCoR) fo r peroxisome proliferator-activated receptor - requires G-protein pathway suppressor 2. J. Biol. Chem. 290, 3666-3679
    • (2015) J. Biol. Chem. , vol.290 , pp. 3666-3679
    • Guo, C.1    Li, Y.2    Gow, C.H.3    Wong, M.4    Zha, J.5    Yan, C.6    Liu, H.7    Wang, Y.8    Burris, T.P.9    Zhang, J.10
  • 14
    • 17044370869 scopus 로고    scopus 로고
    • Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4
    • Zhang, X., Ozawa, Y., Lee, H., Wen, Y. D., Tan, T. H., Wadzinski, B. E., and Seto, E. (2005) Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4. Genes Dev. 19, 827-839
    • (2005) Genes Dev. , vol.19 , pp. 827-839
    • Zhang, X.1    Ozawa, Y.2    Lee, H.3    Wen, Y.D.4    Tan, T.H.5    Wadzinski, B.E.6    Seto, E.7
  • 15
    • 84874221128 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates NCoR to enhance its nuclear translocation and repressive function in human prostate cancer cells
    • Choi, H. K., Yoo, J. Y., Jeong, M. H., Park, S. Y., Shin, D. M., Jang, S. W., Yoon, H. G., and Choi, K. C. (2013) Protein kinase A phosphorylates NCoR to enhance its nuclear translocation and repressive function in human prostate cancer cells. J. Cell. Physiol. 228, 1159-1165
    • (2013) J. Cell. Physiol. , vol.228 , pp. 1159-1165
    • Choi, H.K.1    Yoo, J.Y.2    Jeong, M.H.3    Park, S.Y.4    Shin, D.M.5    Jang, S.W.6    Yoon, H.G.7    Choi, K.C.8
  • 17
    • 40849086600 scopus 로고    scopus 로고
    • TBL1 and TB LR1 phosphorylation on regulated gene promoters overcomes dual CtBP and NCoR/SMRT transcriptional repression checkpoints
    • Perissi, V., Scafoglio, C., Zhang, J., Ohgi, K. A., Rose, D. W., Glass, C. K., and Rosenfeld, M. G. (2008) TBL1 and TB LR1 phosphorylation on regulated gene promoters overcomes dual CtBP and NCoR/SMRT transcriptional repression checkpoints. Mol. Cell 29, 755-766
    • (2008) Mol. Cell , vol.29 , pp. 755-766
    • Perissi, V.1    Scafoglio, C.2    Zhang, J.3    Ohgi, K.A.4    Rose, D.W.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 19
    • 84905978193 scopus 로고    scopus 로고
    • SUMOylation of GPS2 protein regulates its transcription-suppressing function
    • Bi H. Li S. Wang M. Jia Z. Chang A. K. Pang P. Wu, H. 2014 SUMOylation of GPS2 protein regulates its transcription-suppressing function. Mol. Biol. Cell 25 2499-2508
    • (2014) Mol. Biol. Cell , vol.25 , pp. 2499-2508
    • Bi, H.1    Li, S.2    Wang, M.3    Jia, Z.4    Chang, A.K.5    Pang, P.6    Wu, H.7
  • 20
    • 77952315047 scopus 로고    scopus 로고
    • Differential arginine methylation of the G-protein pathway suppressor GPS-2 recognized by tumor-specific T cells in melanoma
    • Jarmalavicius, S., Trefzer, U., and Walden, P. (2010) Differential arginine methylation of the G-protein pathway suppressor GPS-2 recognized by tumor-specific T cells in melanoma. FASEB J. 24, 937-946
    • (2010) FASEB J. , vol.24 , pp. 937-946
    • Jarmalavicius, S.1    Trefzer, U.2    Walden, P.3
  • 22
    • 0030754827 scopus 로고    scopus 로고
    • A human suppressor of c-Jun N-terminal kinase 1 activation by tumor necrosis factor
    • Jin, D. Y., Teramoto, H., Giam, C. Z., Chun, R. F., Gutkind, J. S., and Jeang, K. T. (1997) A human suppressor of c-Jun N-terminal kinase 1 activation by tumor necrosis factor -. J. Biol. Chem. 272, 25816-25823
    • (1997) J. Biol. Chem. , vol.272 , pp. 25816-25823
    • Jin, D.Y.1    Teramoto, H.2    Giam, C.Z.3    Chun, R.F.4    Gutkind, J.S.5    Jeang, K.T.6
  • 23
    • 0034332197 scopus 로고    scopus 로고
    • Coiled-coil motif as a structural basis for the interaction of HTLV type 1 Tax with cellular cofact ors
    • Chun, A. C., Zhou, Y., Wong, C. M., Kung, H. F., Jeang, K. T., and Jin, D. Y. (2000) Coiled-coil motif as a structural basis for the interaction of HTLV type 1 Tax with cellular cofact ors. AIDS Res. Hum. Retroviruses 16, 1689-1694
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , pp. 1689-1694
    • Chun, A.C.1    Zhou, Y.2    Wong, C.M.3    Kung, H.F.4    Jeang, K.T.5    Jin, D.Y.6
  • 24
    • 1342264315 scopus 로고    scopus 로고
    • A corepressor/coactivator exchange complex required for tr anscriptional activation by nuclear receptors and other regulated transcription factors
    • Perissi, V., Aggarwal, A., Glass, C. K., Rose, D. W., and Rosenfeld, M. G. (2004) A corepressor/coactivator exchange complex required for tr anscriptional activation by nuclear receptors and other regulated transcription factors. Cell 116, 511-526
    • (2004) Cell , vol.116 , pp. 511-526
    • Perissi, V.1    Aggarwal, A.2    Glass, C.K.3    Rose, D.W.4    Rosenfeld, M.G.5
  • 25
    • 67649668789 scopus 로고    scopus 로고
    • Transcriptional integration of TLR2 and TLR4 signaling at the NCoR derepression checkpoint
    • Huang, W., Ghisletti, S., Perissi, V., Rosenfeld, M. G., and Glass, C. K. (2009) Transcriptional integration of TLR2 and TLR4 signaling at the NCoR derepression checkpoint. Mol. Cell 35, 48-57
    • (2009) Mol. Cell , vol.35 , pp. 48-57
    • Huang, W.1    Ghisletti, S.2    Perissi, V.3    Rosenfeld, M.G.4    Glass, C.K.5
  • 27
    • 84865322765 scopus 로고    scopus 로고
    • Methods applied to the study of protein arginine methylation
    • Cheng, D., Vemulapalli, V., and Bedford, M. T. (2012) Methods applied to the study of protein arginine methylation. Methods Enzymol. 512, 71-92
    • (2012) Methods Enzymol. , vol.512 , pp. 71-92
    • Cheng, D.1    Vemulapalli, V.2    Bedford, M.T.3
  • 29
    • 0032526024 scopus 로고    scopus 로고
    • Proteasomal regulation of nuclear receptor corepressor-mediated repression
    • Zhang, J., Guenther, M. G., Carthew, R. W., and Lazar, M. A. (1998) Proteasomal regulation of nuclear receptor corepressor-mediated repression. Genes Dev. 12, 1775-1780
    • (1998) Genes Dev. , vol.12 , pp. 1775-1780
    • Zhang, J.1    Guenther, M.G.2    Carthew, R.W.3    Lazar, M.A.4
  • 32
    • 84864673548 scopus 로고    scopus 로고
    • On WD40 proteins: Propelling our knowledge of transcriptional control?
    • Migli ori, V., Mapelli, M., and Guccione, E. (2012) On WD40 proteins: Propelling our knowledge of transcriptional control? Epigenetics 7, 815-822
    • (2012) Epigenetics , vol.7 , pp. 815-822
    • Migliori, V.1    Mapelli, M.2    Guccione, E.3
  • 33
    • 58149295717 scopus 로고    scopus 로고
    • Protein ar ginine methylation in mammals: Who, what, and why
    • Bedford, M. T., and Clarke, S. G. (2009) Protein ar ginine methylation in mammals: Who, what, and why. Mol. Cell 33, 1-13
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 34
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein argi nine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
    • Frankel, A., Yadav, N., Lee, J., Branscombe, T. L., Clarke, S., and Bedford, M. T. (2002) The novel human protein argi nine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277, 3537-3543
    • (2002) J. Biol. Chem. , vol.277 , pp. 3537-3543
    • Frankel, A.1    Yadav, N.2    Lee, J.3    Branscombe, T.L.4    Clarke, S.5    Bedford, M.T.6
  • 35
    • 77952310684 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 6 regulates multiple aspects of gene expression
    • Harrison, M. J., Tang, Y. H., and Dowhan, D. H. (2010) Protein arginine methyltransferase 6 regulates multiple aspects of gene expression. Nucleic Acids Res. 38, 2201-2216
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2201-2216
    • Harrison, M.J.1    Tang, Y.H.2    Dowhan, D.H.3
  • 36
    • 64749109224 scopus 로고    scopus 로고
    • Minireview: Protein arginine methylation of nonhistone proteins in transcriptional regulation
    • Lee, Y. H., and Stallcup, M. R. (2009) Minireview: Protein arginine methylation of nonhistone proteins in transcriptional regulation. Mol. Endocrinol. 23, 425-433
    • (2009) Mol. Endocrinol. , vol.23 , pp. 425-433
    • Lee, Y.H.1    Stallcup, M.R.2
  • 37
    • 0030667739 scopus 로고    scopus 로고
    • Functional interaction of a novel cellular protein with the papillomavirus E2 transactivation domain
    • Breiding, D. E., Sverdrup, F., Grossel, M. J., Moscufo, N., Boonchai, W., and Androphy, E. J. (1997) Functional interaction of a novel cellular protein with the papillomavirus E2 transactivation domain. Mol. Cell. Biol. 17, 7208-7219
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7208-7219
    • Breiding, D.E.1    Sverdrup, F.2    Grossel, M.J.3    Moscufo, N.4    Boonchai, W.5    Androphy, E.J.6
  • 39
    • 0033561038 scopus 로고    scopus 로고
    • Ebi regulates epidermal growth factor receptor signaling pathways in Drosophila
    • Dong, X., Tsuda, L., Zavitz, K. H., Lin, M., Li, S., Carthew, R. W., and Zipursky, S. L. (1999) ebi regulates epidermal growth factor receptor signaling pathways in Drosophila. Genes Dev. 13, 954-965
    • (1999) Genes Dev. , vol.13 , pp. 954-965
    • Dong, X.1    Tsuda, L.2    Zavitz, K.H.3    Lin, M.4    Li, S.5    Carthew, R.W.6    Zipursky, S.L.7
  • 40
    • 0035947080 scopus 로고    scopus 로고
    • Siah-1 SIP, and Ebi collaborate in a novel pathway for-catenin degradation linked to p53 responses
    • Matsuzawa S. I. and Reed, J. C. 2001 Siah-1,SIP, and Ebi collaborate in a novel pathway for-catenin degradation linked to p53 responses. Mol. Cell 7 915-926
    • (2001) Mol. Cell , vol.7 , pp. 915-926
    • Matsuzawa, S.I.1    Reed, J.C.2
  • 42
    • 77956262579 scopus 로고    scopus 로고
    • T he Ski protein negatively regulates Siah2-mediated HDAC3 degradation
    • Zhao, H. L., Ueki, N., and Hayman, M. J. (2010) T he Ski protein negatively regulates Siah2-mediated HDAC3 degradation. Biochem. Biophys. Res. Commun. 399, 623-628
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 623-628
    • Zhao, H.L.1    Ueki, N.2    Hayman, M.J.3
  • 44
    • 79952268280 scopus 로고    scopus 로고
    • Transducin-like protein 1 recruits nuclear factor -B to the target gene promoter for transcriptional activation
    • Ramadoss, S., Li, J., Ding, X., Al Hezaimi, K., and Wang, C. Y. (2011) Transducin -like protein 1 recruits nuclear factor -B to the target gene promoter for transcriptional activation. Mol. Cell. Biol. 31, 924-934
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 924-934
    • Ramadoss, S.1    Li, J.2    Ding, X.3    Al Hezaimi, K.4    Wang, C.Y.5
  • 45
    • 84905581017 scopus 로고    scopus 로고
    • A gain-of-function mouse model identifies PRMT6 as a NF-B coactivator
    • Di Lorenzo, A., Yang, Y., Macaluso, M., and Bedford, M. T. (2014) A gain-of-function mouse model identifies PRMT6 as a NF -B coactivator. Nucleic Acids Res. 42, 8297-8309
    • (2014) Nucleic Acids Res. , vol.42 , pp. 8297-8309
    • Di Lorenzo, A.1    Yang, Y.2    Macaluso, M.3    Bedford, M.T.4
  • 46
    • 84865176464 scopus 로고    scopus 로고
    • Cell cycle regulation by the PRMT6 arginine methyltransferase through repression of cyclin-dependent kinase inhibitors
    • Kleinschmidt, M. A., De Graaf, P., Van Teeffelen, H. A., and Timmers, H. T. (2012) Cell cycle regulation by the PRMT6 arginine methyltransferase through repression of cyclin-dependent kinase inhibitors. PloS ONE 7, e41446
    • (2012) PloS ONE , vol.7 , pp. e41446
    • Kleinschmidt, M.A.1    De Graaf, P.2    Van Teeffelen, H.A.3    Timmers, H.T.4
  • 47
    • 84868121626 scopus 로고    scopus 로고
    • The arginine methyltransferase PRMT6 regulates cell proliferation and senescence through transcriptional repression of tumor suppressor genes
    • Stein, C., Riedl, S., R üthnick, D., Nötzold, R. R., and Bauer, U. M. (2012) The arginine methyltransferase PRMT6 regulates cell proliferation and senescence through transcriptional repression of tumor suppressor genes. Nucleic Acids Res. 40, 9522-9533
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9522-9533
    • Stein, C.1    Riedl, S.2    Rüthnick, D.3    Nötzold, R.R.4    Bauer, U.M.5
  • 48
    • 84868110617 scopus 로고    scopus 로고
    • Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor
    • Neault, M., Mallette, F. A., Vogel, G., Michaud-Levesque, J., and Richard, S. (2012) Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor. Nucleic Acids Res. 40, 9513-9521
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9513-9521
    • Neault, M.1    Mallette, F.A.2    Vogel, G.3    Michaud-Levesque, J.4    Richard, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.